ArticleThe Plant cell2022
Fast and global reorganization of the chloroplast protein biogenesis network during heat acclimation.
Article in The Plant cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 31 citations in OpenAlex.
- Article
- Grain amaranth genes coding for an RNA-binding and a small, unknown function protein, respectively, enhance thermotolerance when overexpressed inPhysiology and molecular biology of plants : an international journal of functional plant biology · 2026Article
- Thermal priming enhances heat tolerance in alfalfa (Medicago sativa L.) through activation of multiple metabolic pathways.BMC plant biology · 2025Article
- Assembly-dependent translational feedback regulation of photosynthetic proteins in land plants.Nature plants · 2025Article
- A truncated variant of the ribosome-associated trigger factor specifically contributes to plant chloroplast ribosome biogenesis.Nature communications · 2025Article
- Golden Gate Cloning for the Standardized Assembly of Gene Elements with Modular Cloning in Chlamydomonas.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Plant PR1 rescues condensation of the plastid iron-sulfur protein by a fungal effector.Nature plants · 2024Article
- STIC2 selectively binds ribosome-nascent chain complexes in the cotranslational sorting of Arabidopsis thylakoid proteins.The EMBO journal · 2024Article
- Chloroplast biogenesis involves spatial coordination of nuclear and organellar gene expression in Chlamydomonas.Plant physiology · 2024Article
- An RNA thermometer in the chloroplast genome of Chlamydomonas facilitates temperature-controlled gene expression.Nucleic acids research · 2023Article
- Fine Tuning of ROS, Redox and Energy Regulatory Systems Associated with the Functions of Chloroplasts and Mitochondria in Plants under Heat Stress.International journal of molecular sciences · 2023Review
- Chloroplast proteostasis: A story of birth, life, and death.Plant communications · 2023Review
- Comparative transcriptomics reveals the role of altered energy metabolism in the establishment of single-cell CFrontiers in plant science · 2023Article
- Retrograde and anterograde signaling in the crosstalk between chloroplast and nucleus.Frontiers in plant science · 2022Review
Corrections and comments
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Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Photosynthesis is a central determinant of plant biomass production, but its homeostasis is increasingly challenged by heat. Little is known about the sensitive regulatory principles involved in heat acclimation that underly the biogenesis and repair of chloroplast-encoded core subunits of photosynthetic complexes. Employing time-resolved ribosome and transcript profiling together with selective ribosome proteomics, we systematically deciphered these processes in chloroplasts of Chlamydomonas reinhardtii. We revealed protein biosynthesis and altered translation elongation as central processes for heat acclimation and showed that these principles are conserved between the alga and the flowering plant Nicotiana tabacum. Short-term heat exposure resulted in specific translational repression of chlorophyll a-containing core antenna proteins of photosystems I and II. Furthermore, translocation of ribosome nascent chain complexes to thylakoid membranes was affected, as reflected by the increased accumulation of stromal cpSRP54-bound ribosomes. The successful recovery of synthesizing these proteins under prolonged acclimation of nonlethal heat conditions was associated with specific changes of the co-translational protein interaction network, including increased ribosome association of chlorophyll biogenesis enzymes and acclimation factors responsible for complex assembly. We hypothesize that co-translational cofactor binding and targeting might be bottlenecks under heat but become optimized upon heat acclimation to sustain correct co-translational protein complex assembly.
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